LYS_MERLU
ID LYS_MERLU Reviewed; 122 AA.
AC P86383;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Lysozyme {ECO:0000303|PubMed:24200802};
DE EC=3.2.1.17 {ECO:0000269|PubMed:24200802};
DE AltName: Full=1,4-beta-N-acetylmuramidase {ECO:0000250|UniProtKB:P83673};
DE AltName: Full=Invertebrate-type lysozyme {ECO:0000305};
OS Meretrix lusoria (Hard clam) (Common Orient clam).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Venerida; Veneroidea; Veneridae; Meretrix.
OX NCBI_TaxID=74491;
RN [1]
RP PROTEIN SEQUENCE (ISOZYMES A AND B), IDENTIFICATION BY MASS SPECTROMETRY,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24200802; DOI=10.1271/bbb.130534;
RA Kuwano Y., Yoneda K., Kawaguchi Y., Araki N., Araki T.;
RT "The complete amino acid sequence and enzymatic properties of an i-type
RT lysozyme isolated from the common orient clam (Meretrix lusoria).";
RL Biosci. Biotechnol. Biochem. 77:2269-2277(2013).
RN [2] {ECO:0007744|PDB:3AYQ}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP DISULFIDE BONDS.
RA Yoneda K., Kuwano Y., Usui T., Ogata M., Suzuki A., Araki T.;
RT "Crystal structure of inhibitor bound lysozyme from Meretrix lusoria.";
RL Submitted (MAY-2011) to the PDB data bank.
RN [3] {ECO:0007744|PDB:3AB6}
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH SUBSTRATE (ISOZYME
RP B), AND DISULFIDE BONDS.
RX PubMed=24192349; DOI=10.1107/s1744309113028170;
RA Kuwano Y., Yoneda K., Kawaguchi Y., Araki T.;
RT "The tertiary structure of an i-type lysozyme isolated from the common
RT orient clam (Meretrix lusoria).";
RL Acta Crystallogr. F 69:1202-1206(2013).
RN [4] {ECO:0007744|PDB:4PJ2}
RP X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX PubMed=25664745; DOI=10.1107/s1399004714025863;
RA Leysen S., Van Herreweghe J.M., Yoneda K., Ogata M., Usui T., Araki T.,
RA Michiels C.W., Strelkov S.V.;
RT "The structure of the proteinaceous inhibitor PliI from Aeromonas
RT hydrophila in complex with its target lysozyme.";
RL Acta Crystallogr. D 71:344-351(2015).
CC -!- FUNCTION: Has bacteriolytic activity against Gram-positive bacteria
CC M.luteus. Also has chitinase activity. {ECO:0000269|PubMed:24200802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000269|PubMed:24200802};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 at 37 degrees Celsius for bacteriolytic activity.
CC Optimum pH is 3 at 40 degrees Celsius for chitinase activity.
CC {ECO:0000269|PubMed:24200802};
CC -!- SUBUNIT: Monomer. {ECO:0000303|PubMed:24200802}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}.
CC -!- MASS SPECTROMETRY: Mass=13376; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:24200802};
CC -!- MISCELLANEOUS: Unlike Ruditapes philippinarum lysozyme, catalytic
CC activity is not affected by variation in salt concentrations.
CC {ECO:0000269|PubMed:24200802}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. Type-I
CC lysozyme subfamily. {ECO:0000255|PROSITE-ProRule:PRU01257}.
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DR PDB; 3AB6; X-ray; 1.78 A; A=1-122.
DR PDB; 3AYQ; X-ray; 1.77 A; A=1-122.
DR PDB; 4PJ2; X-ray; 1.24 A; C/D=1-122.
DR PDBsum; 3AB6; -.
DR PDBsum; 3AYQ; -.
DR PDBsum; 4PJ2; -.
DR AlphaFoldDB; P86383; -.
DR SMR; P86383; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PRIDE; P86383; -.
DR BRENDA; 3.2.1.17; 3231.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd16890; lyz_i; 1.
DR InterPro; IPR008597; Invert_lysozyme.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11195; PTHR11195; 1.
DR Pfam; PF05497; Destabilase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS51909; LYSOZYME_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriolytic enzyme;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Secreted.
FT CHAIN 1..122
FT /note="Lysozyme"
FT /id="PRO_0000389530"
FT DOMAIN 3..118
FT /note="I-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT ACT_SITE 18
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT BINDING 41..47
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT BINDING 93..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT DISULFID 10..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257,
FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT DISULFID 13..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257,
FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT DISULFID 15..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257,
FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT DISULFID 26..35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257,
FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT DISULFID 48..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257,
FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT DISULFID 58..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257,
FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT DISULFID 82..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257,
FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2,
FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ"
FT VARIANT 5
FT /note="I -> T (in isozyme B)"
FT /evidence="ECO:0000269|PubMed:24200802"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:4PJ2"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:4PJ2"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4PJ2"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:4PJ2"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 62..76
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4PJ2"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:4PJ2"
SQ SEQUENCE 122 AA; 13377 MW; 92366099E8AD7881 CRC64;
FAGGIVSQRC LSCICKMESG CRNVGCKMDM GSLSCGYFQI KEAYWIDCGR PGSSWKSCAA
SSYCASLCVQ NYMKRYAKWA GCPLRCEGFA REHNGGPRGC KKGSTIGYWN RLQKISGCHG
VQ
